Theroleofelectrostaticinteractionsinstabilizingthenative state of proteins is controversial. While on the one hand theorists and experimentalists have claimed a crucial role for electrostatic effects in protein unfolding, other s disagree. And while there have been many theoretical simulations of proteins under difference conditions, relatively little attention has been devoted to pH effects. This is due at least in part, to the use of crude electrostatic models (vis, truncated Coulomb) which have prevented the accurate modeling of processes where electrostatic effects dominate using explicit solvent. Our project is focused on the pH-induced unfolding of a protein to form the molten globule state. We have chosen to study alpha-Lactalbumin (GPLA) in its low pH form (A state), the best experimentally characterized molten globule. A. Scientific Subproject